Related Experiment Video
Updated: May 12, 2026

Sample Preparation for Single Virion Atomic Force Microscopy and Super-resolution Fluorescence Imaging
Published on: January 2, 2014
Foamy virus budding and release
Sylvia Hütter1, Irena Zurnic, Dirk Lindemann
1Institute of Virology, Medical Faculty Carl Gustav Carus, Technische Universität Dresden, Fetscherstr. 74, Dresden 01307, Germany. Sylvia.huetter@mailbox.tu-dresden.de
Abstract:
Like all other viruses, a successful egress of functional particles from infected cells is a prerequisite for foamy virus (FV) spread within the host. The budding process of FVs involves steps, which are shared by other retroviruses, such as interaction of the capsid protein with components of cellular vacuolar protein sorting (Vps) machinery via late domains identified in some FV capsid proteins. Additionally, there are features of the FV budding strategy quite unique to the spumaretroviruses. This includes secretion of non-infectious subviral particles and a strict dependence on capsid-glycoprotein interaction for release of infectious virions from the cells. Virus-like particle release is not possible since FV capsid proteins lack a membrane-targeting signal. It is noteworthy that in experimental systems, the important capsid-glycoprotein interaction could be bypassed by fusing heterologous membrane-targeting signals to the capsid protein, thus enabling glycoprotein-independent egress. Aside from that, other systems have been developed to enable envelopment of FV capsids by heterologous Env proteins. In this review article, we will summarize the current knowledge on FV budding, the viral components and their domains involved as well as alternative and artificial ways to promote budding of FV particle structures, a feature important for alteration of target tissue tropism of FV-based gene transfer systems.
Insights
Foamy viruses (FVs) spread via cell budding, utilizing shared retroviral mechanisms and unique spumaretroviral strategies. Understanding FV capsid protein interactions is key for developing novel gene transfer systems.
Area of Science:
- Virology
- Molecular Biology
- Cell Biology
Background:
- Foamy viruses (FVs) are retroviruses essential for host spread via functional particle egress.
- FV budding shares mechanisms with other retroviruses, involving capsid protein interaction with cellular vacuolar protein sorting (Vps) machinery.
- Unique FV budding strategies include secretion of non-infectious subviral particles and dependence on capsid-glycoprotein interaction for infectious virion release.
Purpose of the Study:
- To review current knowledge on foamy virus (FV) budding mechanisms.
- To identify viral components and domains critical for FV particle release.
- To explore alternative and artificial methods for promoting FV particle structure budding.
Main Methods:
- Review of existing literature on foamy virus (FV) biology and retroviral budding processes.
- Analysis of viral components, including capsid proteins and glycoproteins, and their functional domains.
- Examination of experimental systems manipulating FV budding, such as heterologous membrane-targeting signals and Env proteins.
Main Results:
- FV budding involves conserved retroviral pathways and unique spumaretroviral features.
- Capsid-glycoprotein interaction is crucial for infectious FV virion release.
- FV capsid proteins lack intrinsic membrane-targeting signals, preventing virus-like particle release.
- Experimental manipulation can bypass the need for capsid-glycoprotein interaction, enabling glycoprotein-independent egress.
Conclusions:
- Foamy virus (FV) budding is a complex process with both shared and unique retroviral characteristics.
- Understanding FV budding mechanisms is vital for manipulating FV particle release.
- Alternative strategies can facilitate FV particle budding, with implications for FV-based gene transfer systems and target tissue tropism modification.
Related Concept Videos
Pinching-off of Coated Vesicles
What are Viruses?
Retrovirus Life Cycles
Influenza
Vesicular Tubular Clusters
With the help of motor proteins such...
Viral Replication: Lytic Cycle

